ID A0A510DUY9_9CREN Unreviewed; 335 AA. AC A0A510DUY9; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00435}; DE Short=KARI {ECO:0000256|HAMAP-Rule:MF_00435}; DE EC=1.1.1.86 {ECO:0000256|HAMAP-Rule:MF_00435}; DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|HAMAP-Rule:MF_00435}; DE Short=AHIR {ECO:0000256|HAMAP-Rule:MF_00435}; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00435}; GN Name=ilvC {ECO:0000256|HAMAP-Rule:MF_00435}; GN ORFNames=IC006_1298 {ECO:0000313|EMBL:BBG23997.1}; OS Sulfolobus sp. JCM 16833. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus; unclassified Sulfolobus. OX NCBI_TaxID=1294262 {ECO:0000313|EMBL:BBG23997.1}; RN [1] {ECO:0000313|EMBL:BBG23997.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IC-006 {ECO:0000313|EMBL:BBG23997.1}; RA Kato S., Itoh T., Ohkuma M.; RT "Complete Genome Sequencing of Sulfolobus sp. JCM 16833."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino CC acids (BCAA). Catalyzes an alkyl-migration followed by a ketol- CC acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3- CC dihydroxy-isovalerate. In the isomerase reaction, S2AL is CC rearranged via a Mg-dependent methyl migration to produce 3- CC hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, CC this 2-ketoacid undergoes a metal-dependent reduction by NADPH to CC yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000256|HAMAP- CC Rule:MF_00435}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2- CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00435}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)- CC 2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; CC Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, CC ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.86; Evidence={ECO:0000256|HAMAP-Rule:MF_00435}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00435}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00435}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP- CC Rule:MF_00435}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. {ECO:0000256|HAMAP-Rule:MF_00435}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- CC ProRule:PRU01198}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP018929; BBG23997.1; -; Genomic_DNA. DR RefSeq; WP_054845646.1; NZ_BBCL01000003.1. DR GeneID; 41717616; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR HAMAP; MF_00435; IlvC; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013023; KARI. DR InterPro; IPR000506; KARI_C. DR InterPro; IPR013116; KARI_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR21371; PTHR21371; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. DR PROSITE; PS51851; KARI_C; 1. DR PROSITE; PS51850; KARI_N; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00435, KW ECO:0000256|PROSITE-ProRule:PRU01198}; KW Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP- KW Rule:MF_00435, ECO:0000256|PROSITE-ProRule:PRU01198}; KW Isomerase {ECO:0000313|EMBL:BBG23997.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198}; NADP {ECO:0000256|HAMAP-Rule:MF_00435}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198}. FT DOMAIN 5 185 KARI N-terminal Rossmann. FT {ECO:0000259|PROSITE:PS51850}. FT DOMAIN 186 331 KARI C-terminal knotted. FT {ECO:0000259|PROSITE:PS51851}. FT NP_BIND 28 31 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}. FT ACT_SITE 111 111 {ECO:0000256|HAMAP-Rule:MF_00435}. FT METAL 194 194 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 194 194 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 198 198 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 230 230 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT METAL 234 234 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT BINDING 56 56 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}. FT BINDING 137 137 NADP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00435}. FT BINDING 255 255 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00435, ECO:0000256|PROSITE-ProRule: FT PRU01198}. SQ SEQUENCE 335 AA; 36889 MW; E5EDD717F07E845D CRC64; MINIAKIYTD KDASLDALKG KKIAVLGYGN QGRAWALNLR DSGLDVTVGL ERQGKSWEKA TKDGFTPVKT DEAVRNAEVI IFLVPDMIQR TIWLEKVKPN MKKGADLVFA HGFNIHFRMI EPPADSDVYM VAPKGPGDTV RDYYVAGGGV PVLVAAYQNV SGKAMEKALA VAKGIGATRS GALESSFKEE TETDLVGEQT ILVGGIMELM RASFETLVEM GYQPEVAYFE TINEVKMIVD IIHSKGLSGM LRAVSDTAKY GGMTVGKKVI NEDVRKRIRE AAERVRDGQF ASEWVEEYNR GMPTVVNGLK EVDNSLEQKV ANELRDLIER GKPKK //